TPS1_CAMBE
ID TPS1_CAMBE Reviewed; 554 AA.
AC A0A140KFG9;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Hedycaryol synthase {ECO:0000303|PubMed:26744017};
DE EC=4.2.3.174 {ECO:0000269|PubMed:26744017};
DE AltName: Full=(2E,6E)-hedycaryol synthase {ECO:0000305};
DE AltName: Full=Terpene synthase 1 {ECO:0000303|PubMed:26744017};
DE Short=CbTps1 {ECO:0000303|PubMed:26744017};
GN Name=TPS1 {ECO:0000303|PubMed:26744017};
OS Camellia brevistyla.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Theaceae; Camellia.
OX NCBI_TaxID=296050;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=26744017; DOI=10.1007/s00425-015-2454-6;
RA Hattan J., Shindo K., Ito T., Shibuya Y., Watanabe A., Tagaki C., Ohno F.,
RA Sasaki T., Ishii J., Kondo A., Misawa N.;
RT "Identification of a novel hedycaryol synthase gene isolated from Camellia
RT brevistyla flowers and floral scent of Camellia cultivars.";
RL Planta 243:959-972(2016).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC sesquiterpenes and sesquiterpenoid alcohols (PubMed:26744017). Converts
CC farnesyl diphosphate (FPP) to hedycaryol (PubMed:26744017). Hedycaryol
CC is likely to be one of the terpenes that attract insects for
CC pollination of Camellia brevistyla (Probable).
CC {ECO:0000269|PubMed:26744017, ECO:0000305|PubMed:26744017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-hedycaryol +
CC diphosphate; Xref=Rhea:RHEA:54056, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138043, ChEBI:CHEBI:175763;
CC EC=4.2.3.174; Evidence={ECO:0000269|PubMed:26744017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54057;
CC Evidence={ECO:0000269|PubMed:26744017};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in flowers.
CC {ECO:0000269|PubMed:26744017}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; LC070683; BAU68096.1; -; mRNA.
DR AlphaFoldDB; A0A140KFG9; -.
DR SMR; A0A140KFG9; -.
DR KEGG; ag:BAU68096; -.
DR BRENDA; 4.2.3.174; 15336.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..554
FT /note="Hedycaryol synthase"
FT /id="PRO_0000452462"
FT MOTIF 307..311
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 270
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 449
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 452
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 554 AA; 64001 MW; 2AF4D52D433E2649 CRC64;
MASSQVGDMV NGNAEPTRHL AKFPPSLWGD RFTSFTLDKQ LWDKYGNEIE VLKEQVRSMV
VAGGRKAAEQ INLINVLERL GVSYHFEKEI EEQLEQLFAK FEDNEDYDLF TIALHFRIFR
QHGYKMSCDV FNKFRDSNGE FKETVSNDVR GMLSLYEATY LKIRGEGFLD EAHAFTIAQL
ESLVGGPHLS SDLSEQVMHA LKQSIHRGFP RLEAKHFISF YEKDAARNET LLRLAKLDFN
QLQLSHREEL CHIFRWWKEL DLISKVPYAR DRAVECFFWS TCAYYEPQHS VGRAVLTKIV
LLLSVTDDTY DAYGTYDELK LYTNAVQRWD ASAMDELPDY MKTLYRALLN VYDEVERDLA
KQGRAYGVHH SKEAFKEIVR SYEIEAEWFK EGYVASFEEY MKNALVTSTG RLHTTSCFMG
LEADVATTEA FEWILTKPKM VAASGAIGRL VDDVMSNDEE QERGHVATGL DCYMKQHGVS
KQEAIVELYK MIENAWRDIN EEMLKPTAIS MKLLIHVLNL SRISDVVYKY VDGYTHPEII
KDHVISLFED PIPM
